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dc.contributor.authorSwiatek, Agnieszka
dc.contributor.authorMacNeill, Stuart Andrew
dc.date.accessioned2010-10-20T11:04:31Z
dc.date.available2010-10-20T11:04:32Z
dc.date.issued2010-04-12
dc.identifier.citationSwiatek , A & MacNeill , S A 2010 , ' The archaeo-eukaryotic GINS proteins and the archaeal primase catalytic subunit PriS share a common domain ' , Biology Direct , vol. 5 , no. 1 , pp. 17 . https://doi.org/10.1186/1745-6150-5-17en
dc.identifier.issn1745-6150
dc.identifier.otherPURE: 1751910
dc.identifier.otherPURE UUID: 912ee3a4-5038-4bb8-9bc8-7f145d364564
dc.identifier.otherScopus: 77950637780
dc.identifier.otherORCID: /0000-0002-0555-0007/work/39107844
dc.identifier.urihttp://hdl.handle.net/10023/1047
dc.descriptionThis work was funded by the Scottish Universities Life Sciences Alliance (SULSA).en
dc.description.abstractPrimase and GINS are essential factors for chromosomal DNA replication in eukaryotic and archaeal cells. Here we describe a previously undetected relationship between the C-terminal domain of the catalytic subunit (PriS) of archaeal primase and the B-domains of the archaeo-eukaryotic GINS proteins in the form of a conserved structural domain comprising a three-stranded antiparallel beta-sheet adjacent to an alpha-helix and a two-stranded beta-sheet or hairpin. The presence of a shared domain in archaeal PriS and GINS proteins, the genes for which are often found adjacent on the chromosome, suggests simple mechanisms for the evolution of these proteins.
dc.format.extent6
dc.language.isoeng
dc.relation.ispartofBiology Directen
dc.rightsThis is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.en
dc.subjectQH301 Biologyen
dc.subject.lccQH301en
dc.titleThe archaeo-eukaryotic GINS proteins and the archaeal primase catalytic subunit PriS share a common domainen
dc.typeJournal articleen
dc.description.versionPublisher PDFen
dc.contributor.institutionUniversity of St Andrews.School of Biologyen
dc.contributor.institutionUniversity of St Andrews.Biomedical Sciences Research Complexen
dc.identifier.doihttps://doi.org/10.1186/1745-6150-5-17
dc.description.statusPeer revieweden
dc.identifier.urlhttp://www.scopus.com/inward/record.url?scp=77950637780&partnerID=8YFLogxKen
dc.identifier.urlhttp://www.biology-direct.com/content/5/1/17en


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